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G3V801

- NETR_RAT

UniProt

G3V801 - NETR_RAT

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Protein

Neurotrypsin

Gene

Prss12

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei516 – 5172Reactive bond homologSequence Analysis
Active sitei562 – 5621Charge relay systemBy similarity
Active sitei612 – 6121Charge relay systemBy similarity
Active sitei711 – 7111Charge relay systemBy similarity

GO - Molecular functioni

  1. scavenger receptor activity Source: InterPro
  2. serine-type endopeptidase activity Source: Ensembl

GO - Biological processi

  1. exocytosis Source: UniProtKB
  2. zymogen activation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Protein family/group databases

MEROPSiS01.237.

Names & Taxonomyi

Protein namesi
Recommended name:
Neurotrypsin (EC:3.4.21.-)
Alternative name(s):
Serine protease 12
Gene namesi
Name:Prss12
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi69238. Prss12.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. axon Source: UniProtKB
  2. cytoplasmic vesicle Source: Ensembl
  3. dendrite Source: Ensembl
  4. extracellular region Source: UniProtKB-KW
  5. plasma membrane Source: UniProtKB
  6. synaptic cleft Source: Ensembl
  7. terminal bouton Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 761740NeurotrypsinPRO_0000416843Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi85 ↔ 1571 Publication
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi101 ↔ 1411 Publication
Disulfide bondi130 ↔ 1551 Publication
Disulfide bondi191 ↔ 255By similarity
Disulfide bondi204 ↔ 265By similarity
Disulfide bondi235 ↔ 245By similarity
Disulfide bondi298 ↔ 361By similarity
Disulfide bondi311 ↔ 371By similarity
Disulfide bondi341 ↔ 351By similarity
Disulfide bondi411 ↔ 475By similarity
Disulfide bondi424 ↔ 485By similarity
Disulfide bondi455 ↔ 465By similarity
Disulfide bondi505 ↔ 636Sequence Analysis
Glycosylationi521 – 5211N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi547 ↔ 563By similarity
Glycosylationi569 – 5691N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi651 ↔ 717By similarity
Disulfide bondi680 ↔ 694By similarity
Disulfide bondi707 ↔ 736By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021116.

Structurei

Secondary structure

1
761
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi92 – 954Combined sources
Beta strandi98 – 1014Combined sources
Helixi104 – 1063Combined sources
Helixi119 – 1213Combined sources
Beta strandi131 – 1344Combined sources
Turni135 – 1373Combined sources
Beta strandi138 – 1447Combined sources
Beta strandi150 – 1545Combined sources
Beta strandi156 – 1583Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K4RNMR-A84-160[»]
2K51NMR-A84-160[»]
ProteinModelPortaliG3V801.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini85 – 15773KringlePROSITE-ProRule annotationAdd
BLAST
Domaini166 – 267102SRCR 1PROSITE-ProRule annotationAdd
BLAST
Domaini273 – 373101SRCR 2PROSITE-ProRule annotationAdd
BLAST
Domaini386 – 487102SRCR 3PROSITE-ProRule annotationAdd
BLAST
Domaini517 – 760244Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni505 – 51612Zymogen activation regionBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 kringle domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
Contains 3 SRCR domains.PROSITE-ProRule annotation

Keywords - Domaini

Kringle, Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118953.
HOGENOMiHOG000113767.
InParanoidiG3V801.
KOiK09624.
OMAiDDGWTDK.
OrthoDBiEOG7RNK07.
PhylomeDBiG3V801.
TreeFamiTF329295.

Family and domain databases

Gene3Di2.40.20.10. 1 hit.
3.10.250.10. 3 hits.
InterProiIPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00051. Kringle. 1 hit.
PF00530. SRCR. 3 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSiPR00722. CHYMOTRYPSIN.
PR00258. SPERACTRCPTR.
SMARTiSM00130. KR. 1 hit.
SM00202. SR. 3 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 3 hits.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00021. KRINGLE_1. 1 hit.
PS50070. KRINGLE_2. 1 hit.
PS00420. SRCR_1. 3 hits.
PS50287. SRCR_2. 3 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

G3V801 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALARCVLAV ILGVLSEVAR ADPVLHSPLH RPHPSPPRSQ HAHYLPSSRR
60 70 80 90 100
PPRTPRFPLP PRAPAAQRPQ LLSTRHTPPT ISRRCGAGEP WGNATNLGVP
110 120 130 140 150
CLHWDEVPPF LERSPPASWA ELRGQPHNFC RSPGGAGRPW CFYRNAQGKV
160 170 180 190 200
DWGYCDCGQG PALPVIRLVG GKSGHEGRVE LYHAGQWGTI CDDQWDDADA
210 220 230 240 250
EVICRQLGLS GIAKAWHQAH FGEGSGPILL DEVRCTGNEL SIEQCPKSSW
260 270 280 290 300
GEHNCGHKED AGVSCAPLTD GVIRLSGGKS VHEGRLEVYY RGQWGTVCDD
310 320 330 340 350
GWTEMNTYVA CRLLGFKYGK QSSVNHFEGS SRPIWLDDVS CSGKEASFIQ
360 370 380 390 400
CSRRQWGRHD CSHREDVGLT CYPDSDGHRL SPGFPIRLMD GENKREGRVE
410 420 430 440 450
VFVSGQWGTI CDDGWTDKHA AVICRQLGYK GPARARTMAY FGEGKGPIHM
460 470 480 490 500
DNVKCTGNEK ALADCVKQDI GRHNCRHSED AGVICDYYEK KTSGHGNKET
510 520 530 540 550
LSSGCGLRLL HRRQKRIIGG NNSLRGAWPW QASLRLKSTH GDGRLLCGAT
560 570 580 590 600
LLSSCWVLTA AHCFKRYGNN SRSYAVRVGD YHTLVPEEFE QEIGVQQIVI
610 620 630 640 650
HRNYRPDSSD YDIALVRLQG SGEQCARLST HVLPACLPLW RERPQKTASN
660 670 680 690 700
CHITGWGDTG RAYSRTLQQA AVPLLPKRFC KERYKGLFTG RMLCAGNLQE
710 720 730 740 750
DNRVDSCQGD SGGPLMCEKP DETWVVYGVT SWGYGCGIKD TPGVYTRVPA
760
FVPWIKSVTS L
Length:761
Mass (Da):84,220
Last modified:November 16, 2011 - v1
Checksum:i215EE73A3CE468EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1341G → D in CAC35028. 1 PublicationCurated
Sequence conflicti404 – 4041S → N in CAC35028. 1 PublicationCurated
Sequence conflicti515 – 5151K → T in CAC35028. 1 PublicationCurated
Sequence conflicti565 – 5651K → T in CAC35028. 1 PublicationCurated
Sequence conflicti588 – 5881E → G in CAC35028. 1 PublicationCurated
Sequence conflicti592 – 5921E → D in CAC35028. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ311671 mRNA. Translation: CAC35028.2.
CH473952 Genomic DNA. Translation: EDL82129.1.
RefSeqiNP_445956.1. NM_053504.1.
UniGeneiRn.86653.

Genome annotation databases

EnsembliENSRNOT00000021116; ENSRNOP00000021116; ENSRNOG00000015353.
GeneIDi85266.
KEGGirno:85266.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ311671 mRNA. Translation: CAC35028.2 .
CH473952 Genomic DNA. Translation: EDL82129.1 .
RefSeqi NP_445956.1. NM_053504.1.
UniGenei Rn.86653.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2K4R NMR - A 84-160 [» ]
2K51 NMR - A 84-160 [» ]
ProteinModelPortali G3V801.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000021116.

Protein family/group databases

MEROPSi S01.237.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000021116 ; ENSRNOP00000021116 ; ENSRNOG00000015353 .
GeneIDi 85266.
KEGGi rno:85266.

Organism-specific databases

CTDi 8492.
RGDi 69238. Prss12.

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00760000118953.
HOGENOMi HOG000113767.
InParanoidi G3V801.
KOi K09624.
OMAi DDGWTDK.
OrthoDBi EOG7RNK07.
PhylomeDBi G3V801.
TreeFami TF329295.

Miscellaneous databases

NextBioi 617408.
PROi G3V801.

Family and domain databases

Gene3Di 2.40.20.10. 1 hit.
3.10.250.10. 3 hits.
InterProi IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR001190. SRCR.
IPR017448. SRCR-like_dom.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00051. Kringle. 1 hit.
PF00530. SRCR. 3 hits.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PRINTSi PR00722. CHYMOTRYPSIN.
PR00258. SPERACTRCPTR.
SMARTi SM00130. KR. 1 hit.
SM00202. SR. 3 hits.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF56487. SSF56487. 3 hits.
SSF57440. SSF57440. 1 hit.
PROSITEi PS00021. KRINGLE_1. 1 hit.
PS50070. KRINGLE_2. 1 hit.
PS00420. SRCR_1. 3 hits.
PS50287. SRCR_2. 3 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of the cDNA encoding rat neurotrypsin."
    Hintsch G., Sonderegger P.
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  4. Cited for: STRUCTURE BY NMR OF 84-160, PARTIAL PROTEIN SEQUENCE, DISULFIDE BOND, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiNETR_RAT
AccessioniPrimary (citable) accession number: G3V801
Secondary accession number(s): Q99JC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 18, 2012
Last sequence update: November 16, 2011
Last modified: October 29, 2014
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3